Protein Family Models

This domain is found towards the C terminus of Beta-glucuronidase from Formosa agariphila (P17_GH2) and similar proteins mainly from bacteria and fungi. P17_GH2 is involved in the degradation of the polysaccharide ulvan. The function of this domain, which shows an all-beta structure, is unknown [1]. [1]. 31285597. A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan. Reisky L, Prechoux A, Zuhlke MK, Baumgen M, Robb CS, Gerlach N, Roret T, Stanetty C, Larocque R, Michel G, Song T, Markert S, Unfried F, Mihovilovic MD, Trautwein-Schult A, Becher D, Schweder T, Bornscheuer UT, Hehemann JH;. Nat Chem Biol. 2019;15:803-812. (from Pfam)

Date:

2024-10-16

This domain is found in a number of proteins belonging to glycosyl hydrolase 2 family [1-5]. Paper describing PDB structure 1bhg. [1]. 8599764. Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs. Jain S, Drendel WB, Chen ZW, Mathews FS, Sly WS, Grubb JH;. Nat Struct Biol. 1996;3:375-381. Paper describing PDB structure 1dp0. [2]. 11045615. High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation. Juers DH, Jacobson RH, Wigley D, Zhang XJ, Huber RE, Tronrud DE, Matthews BW;. Protein Sci. 2000;9:1685-1699. Paper describing PDB structure 1jyn. [3]. 11732897. A structural view of the action of Escherichia coli (lacZ) beta-galactosidase. Juers DH, Heightman TD, Vasella A, McCarter JD, Mackenzie L, Withers SG, Matthews BW;. Biochemistry. 2001;40:14781-14794. Paper describing PDB structure 1px3. [4]. 14621996. Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase. Juers DH, Hakda S, Matthews BW, Huber RE;. Biochemistry. 2003;42:13505-13511. Paper describing PDB structure 1yq2. [5]. 16171818. Cold-active beta-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1.9A resolution. Skalova T, Dohnalek J, Spiwok V, Lipovova P, Vondrackova E, Petrokova H, Duskova J, Strnad H, Kralova B, Hasek J;. J Mol Biol. 2005;353:282-294. (from Pfam)

Date:

2024-10-16

Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognises and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186. NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan [1]. [1]. 18524852. Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation. Schallus T, Jaeckh C, Feher K, Palma AS, Liu Y, Simpson JC, Mackeen M, Stier G, Gibson TJ, Feizi T, Pieler T, Muhle-Goll C;. Mol Biol Cell. 2008;19:3404-3414. (from Pfam)

Date:

2024-10-16

This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. [1]. 8008071. Three-dimensional structure of beta-galactosidase from E. coli. Jacobson RH, Zhang XJ, DuBose RF, Matthews BW;. Nature. 1994;369:761-766. (from Pfam)

Date:

2024-10-16

This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction. [1]. 8008071. Three-dimensional structure of beta-galactosidase from E. coli. Jacobson RH, Zhang XJ, DuBose RF, Matthews BW;. Nature. 1994;369:761-766. (from Pfam)

Date:

2024-10-16

This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. [1]. 8008071. Three-dimensional structure of beta-galactosidase from E. coli. Jacobson RH, Zhang XJ, DuBose RF, Matthews BW;. Nature. 1994;369:761-766. (from Pfam)

Date:

2024-10-16